Informacja

Drogi użytkowniku, aplikacja do prawidłowego działania wymaga obsługi JavaScript. Proszę włącz obsługę JavaScript w Twojej przeglądarce.

English (EN)·Polski (PL)·Yкраїнський (UK)
Przejdź do strony domowej biblioteki Centralna Biblioteka Wojskowa Link otwiera się w nowym oknie Logo biblioteki Prolib Integro - strona głównaCentralna Biblioteka Wojskowa

Wyszukujesz frazę "baculovirus" wg kryterium: Wszystkie pola

  Lista filtrów
Wyrównaj
    Wyświetlanie 1-4 z 4
    Tytuł:
    Recombinant VP60 in the form of virion-like particles as a potential vaccine against rabbit hemorrhagic disease virus*
    Autorzy:
    Gromadzka, Beata
    Szewczyk, Bogusław
    Konopa, Grażyna
    Fitzner, Andrzej
    Kęsy, Andrzej
    Powiązania:
    https://bibliotekanauki.pl/articles/1041251.pdf
    Data publikacji:
    2006
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    baculovirus
    VLP
    RHDV
    VP60
    Opis:
    Rabbit hemorrhagic disease virus (RHDV) which causes a highly contagious disease of wild and domestic rabbits belongs to the family Caliciviridae. It is a small, positive single-stranded RNA virus with a genome of 7.5 kb and has a diameter of approximately 40 nm. In negatively stained electron micrographs the virus shows typical calicivirus morphology with regularly arranged cup-shaped structures on the surface. It is a major pathogen of rabbits in many countries. Vp60 - a coat protein of molecular mass around 60 kDa is the major antigen of RHDV. It is present as 90 dimeric units per virion particle. We have expressed VP60 gene in the baculovirus system with the aim to use it as a potential vaccine against RHDV and a diagnostic reagent in immunological tests. cDNA of the vp60 gene of strain SGM, was cloned into a baculovirus transfer vector as full-length gene, as well as truncated gene lacking 600 5´-terminal nucleotides. The sequence of SGM VP60 differed markedly from that of the reference strain. Full-length recombinant VP60 protein from the SGM strain self-assembled to form virus-like particles (VLPs). These particles observed by electron microscopy were morphologically similar to native virions and were able to agglutinate human group 0 erythrocytes. After immunization the recombinant particles induced RHDV-specific antibodies in rabbits and guinea pigs. Rabbits immunized with the VLPs were fully protected against challenge with a virulent RHDV.
    Źródło:
    Acta Biochimica Polonica; 2006, 53, 2; 371-376
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    Characterization of recombinant expression of Bombyx mori bidensovirus ns1 using a modified vector
    Autorzy:
    Li, Guohui
    Li, Mangmang
    Wang, Peng
    Hu, Zhaoyang
    Yao, Qin
    Tang, Qi
    Chen, Keping
    Powiązania:
    https://bibliotekanauki.pl/articles/1039216.pdf
    Data publikacji:
    2014
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    BmBDV
    NS1
    baculovirus expression vector
    Sf9
    egfp
    Opis:
    ns1 gene of Bombyx mori bidensovirus (BmBDV) consisted of 951 nucleotides encoding a deduced 316-amino aicd protein. In this study, the gene was cloned and fused in frame with a N-terminal 6×His tag under control of the polyhedrin promoter, which was transposed into the mini-attTn7 locus of a modified baculovirus vector. Transfection of Sf-9 cells with the resulting recombinant DNA was performed to prepare recombinant virus and the resultant supernatant of transfection with fluorescent signal was harvested. Western blot analysis revealed that NS1 protein was successfully expressed in Sf9 cells infected with the recombinant virus and was confirmed by LC-MS/MS analysis. Moreover, the expressed NS1 is a phosphorylated protein and the phosphorylation site is Thr-184. These results showed that the activity of BmBDV NS1 may be regulated by phosphorylation.
    Źródło:
    Acta Biochimica Polonica; 2014, 61, 4; 787-794
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    Advantage of a baculovirus expression system for protein-protein interaction studies. Involvement of posttranslational phosphorylation in the interaction between wt p53 protein and poly(ADP-ribose) polymerase-1
    Autorzy:
    Schmid, Gerald
    Wojciechowski, Jacek
    Węsierska-Gądek, Józefa
    Powiązania:
    https://bibliotekanauki.pl/articles/1041382.pdf
    Data publikacji:
    2005
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    nucleocytoplasmic shuttling
    NES
    p53 isomers
    p53 stability
    cell cycle arrest
    2D-PAGE
    p53 nuclear export
    FACS analysis
    p53 pull-down assay
    p53 phosphorylation
    Opis:
    We recently observed an interaction between poly(ADP-ribose) polymerase-1 (PARP-1) and the tumor suppressor p53 protein. However, more extensive studies on both proteins, especially those on characterization of their domains involved in the interaction were difficult due to very low expression levels of p53 in mammalian cells. Therefore, we generated recombinant proteins for such studies. To clarify which domains of human PARP-1 and of human wild-type (wt) p53 were involved in this protein-protein interaction, we generated baculoviral constructs encoding full length or distinct functional domains of both proteins. Full length PARP-1 was simultaneously coexpressed in insect cells with full length wt p53 protein or its distinct truncated fragments and vice versa. Reciprocal immunoprecipitation of Sf9 cell lysates revealed that the central and carboxy-terminal fragments of p53 each were sufficient to confer binding to PARP-1, whereas the amino-terminal part harbouring the transactivation functional domain was dispensable. On the other hand, the amino-terminal and central fragments of PARP-1 were both necessary for complex formation with p53 protein. Since the most important features of p53 protein are regulated by phosphorylation, we addressed the question whether its phosphorylation is essential for the binding between the two proteins. Baculovirally expressed wt p53 was post-translationally modified. At least six distinct p53 isomers were resolved by immunoblotting following two-dimensional separation of baculovirally expressed wt p53 protein. Using specific phospho-serine antibodies, we identified phosphorylation of baculovirally expressed p53 protein at five distinct sites. To define the role of p53 phosphorylation, pull-down assays using untreated and dephosphorylated p53 protein were performed. Dephosphorylated p53 failed to bind PARP-1, indicating that complex formation between the two proteins was regulated by phosphorylation of p53. The marked phosphorylation of p53 at Ser392 observed in unstressed cells suggests that the phosphorylated carboxy-terminal part of p53 undergoes complex formation with PARP-1 resulting in masking of the NES and thereby preventing its export.
    Źródło:
    Acta Biochimica Polonica; 2005, 52, 3; 713-719
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
      Wyświetlanie 1-4 z 4

      Ta witryna wykorzystuje pliki cookies do przechowywania informacji na Twoim komputerze. Pliki cookies stosujemy w celu świadczenia usług na najwyższym poziomie, w tym w sposób dostosowany do indywidualnych potrzeb. Korzystanie z witryny bez zmiany ustawień dotyczących cookies oznacza, że będą one zamieszczane w Twoim komputerze. W każdym momencie możesz dokonać zmiany ustawień dotyczących cookies